ABSTRACT: The incorporation of 14C amino acids into protein by Alcaligenes faecalis fragments has been demonstrated. Using 14C valine, it was found that most of the incorporated amino acid was within the peptide chains. Alcaligenes fragments have been partially solubilized by treatment with perfluoro octanoate without affecting the incorporation activity. The soluble fraction obtained after this treatment can be replaced by purified “amino acid incorporation enzymes”.

ABSTRACT: Indications have been obtained for the presence ot the amino acid incorporation enzyme in the supernatant fraction from rat liver and in the precipitate obtained by acidification of this fraction to pH 5.2 (pH 5 enzymes). Highly purified amino acid incorporation enzyme from A. faecalis completely replaces the pH 5 enzymes in stimulating the incorporation of C14-leucine into protein of rat livermicrosomes. These observations show that the amino acid incorporation enzyme is involved in protein biosyntheses of both mammalian and bacterial cells.
Highly purified preparations of the A. faecalis incorporation enzyme catalyze a rapid, Mg++dependent exchange a radioactive ADP with ATP an activity which appears to be related to their amino acid incorporation activity. This finding may be of significance, since glutathione synthetase, which catalyzes the synthesis of a typical peptide, brings about a similar exchange.

ABSTRACT: Particulate preparations of Alcaligenes faecalis, consisting largely of cell membrane fragments, incorporate amino acids into their proteins. This incorporation, which appears to reflect protein biosynthesis, is driven by oxidative phosphorylation and is stimulated by an enzyme, present in the supernatant extract, which has been isolated in highly purified form. The purified enzyme is free of activating enzymes catalyzing the amino acid-dependent exchange of PP32 with ATP and the same seems to be true of the bacterial particles.

ABSTRACT: Molecules containing porphyric groupe do not influence the photo-restoration of E. Coli strains studied by the authors. In consequence, in the case of these strains : a) The porphyrins do not appreciably act as chromophores in the photo-restoration process. This fact should be discussed as soon as a sufficiently precise action spectrum of light on E. Coli will be available. b) The catalase and peroxydase enzymes do not appreciably participate in the photo-restoration process, which remains indefinite. We can only state that this process does not apply to lesions due to the activity of photo-formed peroxydes. So it seems that photo-restoration is very different from restoration by catalase, which is an essentially peroxydase process.